ID   PENF_STREX              Reviewed;         275 AA.
AC   E3VWK2;
DT   03-APR-2013, integrated into UniProtKB/Swiss-Prot.
DT   11-JAN-2011, sequence version 1.
DT   03-AUG-2022, entry version 26.
DE   RecName: Full=1-deoxy-11-beta-hydroxypentalenate dehydrogenase;
DE            EC=1.1.1.340;
DE   AltName: Full=Pentalenolactone biosynthesis protein F;
GN   Name=penF;
OS   Streptomyces exfoliatus (Streptomyces hydrogenans).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1905;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=UC5319;
RX   PubMed=21284395; DOI=10.1021/ja111279h;
RA   Zhu D., Seo M.J., Ikeda H., Cane D.E.;
RT   "Genome mining in streptomyces. Discovery of an unprecedented P450-
RT   catalyzed oxidative rearrangement that is the final step in the
RT   biosynthesis of pentalenolactone.";
RL   J. Am. Chem. Soc. 133:2128-2131(2011).
CC   -!- FUNCTION: Catalyzes the oxidation of 1-deoxy-11-beta-hydroxypentalenic
CC       acid to 1-deoxy-11-oxopentalenic acid in the biosynthesis of
CC       pentalenolactone antibiotic. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-deoxy-11beta-hydroxypentalenate + NAD(+) = 1-deoxy-11-
CC         oxopentalenate + H(+) + NADH; Xref=Rhea:RHEA:34559,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC         ChEBI:CHEBI:70779, ChEBI:CHEBI:70780; EC=1.1.1.340;
CC   -!- PATHWAY: Antibiotic biosynthesis; pentalenolactone biosynthesis.
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC       family. {ECO:0000305}.
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DR   EMBL; HQ292066; ADO85590.1; -; Genomic_DNA.
DR   AlphaFoldDB; E3VWK2; -.
DR   SMR; E3VWK2; -.
DR   BioCyc; MetaCyc:MON-16848; -.
DR   UniPathway; UPA00974; -.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR   InterPro; IPR002347; SDR_fam.
DR   Pfam; PF00106; adh_short; 1.
DR   PRINTS; PR00081; GDHRDH.
DR   PRINTS; PR00080; SDRFAMILY.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   PROSITE; PS00061; ADH_SHORT; 1.
PE   3: Inferred from homology;
KW   Antibiotic biosynthesis; NAD; Oxidoreductase.
FT   CHAIN           1..275
FT                   /note="1-deoxy-11-beta-hydroxypentalenate dehydrogenase"
FT                   /id="PRO_0000421998"
FT   ACT_SITE        157
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT   BINDING         12..36
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         144
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         161
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   275 AA;  29203 MW;  EA88E74926E16317 CRC64;
     MHLQTRAAVV TGAASGIGLA LSARFARAGA GVVMADVDGD ALHRRAAELT ARGAQVTAVT
     ADLTDPEVVE RLADTAFDQL GDIDVVCNNA GVLGPVGQPL WEVPLERMRQ VFEVNHWAHV
     LVARAFVPRL LERGRPAHLI HTASMSAFVV GAGSAAYAAS KHADLAVARS LRADLRGTGV
     RVSVLCPGRV DTPMVQGLTA PRGAGGDTSV SAEDVAGLVW EALGSDRFYL FSNSDARIRL
     RDQFDDVWRH VSLPPPSPEE ELWPAPKATT VTMNH